Primary Information |
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BoMiProt ID | Bomi209 |
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Protein Name | Aspartoacylase |
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Organism | Bos taurus |
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Uniprot ID | P46446 |
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Milk Fraction | Exosome |
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Aminoacid Length | 313 |
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Molecular Weight | 35738 |
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FASTA Sequence |
Download |
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Gene Name | ASPA |
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Protein Existence Status | Reviewed: Experimental evidence at protein level |
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Secondary Information |
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Presence in other biological fluids/tissue/cells | first partially purified from rat brain
and was then subsequently purified to homogeneity from
bovine brain; distributed
primarily in the oligodendrocytes |
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Protein Function | catalyzes the deacetylation of N-acetylaspartic acid (NAA) to produce acetate
and L-aspartate; the metabolism of NAA
appears to be necessary in the formation of myelin lipids, and defects in this enzyme lead to Canavan
disease, a fatal neurological disorder. Aspartoacylase catalyzes hydrolysis of N-acetyl-l-aspartate to aspartate and acetate in the vertebrate brain. |
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Biochemical Properties | zinc-dependent peptidase; essential metal ion ligands and active-site functional
groups of the carboxypeptidases are conserved in the
aspartoacylases; Divalent cations are reported to activate the
enzyme, but the addition of these cations lead to only modest
increases in catalytic activity; not a metalloenzyme |
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PTMs | A putative N-glycosylation
site (Asn117) contained in an Asn-X-Thr/Ser
recognition sequence; located adjacent to one of the proposed histidine metal
ion ligands |
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Site(s) of PTM(s)
N-glycosylation,
O-glycosylation,
Phosphorylation
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Predicted Disorder Regions | NA |
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DisProt Annotation | |
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TM Helix Prediction | No TM helices |
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Significance of PTMs | enzyme activity has
been hypothesized to be regulated both by glycosylation and
by phosphorylation/dephosphorylation |
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Additional Comments | Mutations that result in near undetectable activity of aspartoacylase, which catalyzes the deacetylation of N-acetyl-l-aspartate, correlate with Canavan Disease, a neurodegenerative disorder usually fatal during childhood. |
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Bibliography | 1. Le Coq, J., An, H.-J., Lebrilla, C., & Viola, R. E. (2006). Characterization of human aspartoacylase: the brain enzyme responsible for Canavan disease. Biochemistry, 45(18), 5878–5884. https://doi.org/10.1021/bi052608w. 2.Hershfield JR, Pattabiraman N, Madhavarao CN, Namboodiri MA. Mutational analysis of aspartoacylase: implications for Canavan disease. Brain Res. 2007 May 7;1148:1-14. doi: 10.1016/j.brainres.2007.02.069. Epub 2007 Mar 3. PMID: 17391648; PMCID: PMC1933483. |